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金属离子在酿酒酵母钾离子激活型醛脱氢酶作用机制中的作用。

The role of the metal ion in the mechanism of the K+-activated aldehyde dehydrogenase of Saccharomyces cerevisiae.

作者信息

Dickinson F M, Haywood G W

机构信息

Department of Biochemistry, University of Hull, U.K.

出版信息

Biochem J. 1987 Oct 15;247(2):377-84. doi: 10.1042/bj2470377.

Abstract

The effect of K+ on assays of the enzyme was studied and it appears that the activation occurs slowly by a two-step process. Kinetic measurements suggest that the enzyme-catalysed reaction can proceed slowly (0.4%) in the complete absence of K+. The enzyme exhibits a K+-activated esterase activity, which is further activated by NAD+ or NADH. Stopped-flow studies indicated that the principal effect of K+ on the dehydrogenase reaction is to accelerate a step (possibly acyl-enzyme hydrolysis) associated with a fluorescence and small absorbance transient that occurs after hydride transfer and before NADH dissociation from the terminal E-NADH complex. The variation of activity of the enzyme with pH was studied. An enzyme group with pKa approx. 7.1 apparently promotes enzyme activity when in its alkaline form.

摘要

研究了钾离子对该酶测定的影响,结果表明激活过程是通过两步缓慢发生的。动力学测量表明,在完全没有钾离子的情况下,酶催化反应仍能缓慢进行(0.4%)。该酶具有钾离子激活的酯酶活性,且这种活性会被烟酰胺腺嘌呤二核苷酸(NAD⁺)或烟酰胺腺嘌呤二核苷酸磷酸(NADH)进一步激活。停流研究表明,钾离子对脱氢酶反应的主要作用是加速一个步骤(可能是酰基酶水解),该步骤与氢化物转移后、NADH从末端E-NADH复合物解离前出现的荧光和小吸光度瞬变有关。研究了该酶活性随pH值的变化。一个pKa约为7.1的酶基团在其碱性形式时显然能促进酶活性。

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本文引用的文献

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The kinetics of the alpha-chymotrypsin-catalyzed hydrolysis of p-nitrophenyl acetate.
Biochemistry. 1962 Nov;1:1097-106. doi: 10.1021/bi00912a021.
2
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Biochem J. 1962 Aug;84(2):244-54. doi: 10.1042/bj0840244.
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